ID K9PIE8_9CYAN Unreviewed; 119 AA.
AC K9PIE8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit M {ECO:0000256|HAMAP-Rule:MF_01352};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01352};
DE AltName: Full=NAD(P)H dehydrogenase I subunit M {ECO:0000256|HAMAP-Rule:MF_01352};
DE Short=NDH-1 subunit M {ECO:0000256|HAMAP-Rule:MF_01352};
DE Short=NDH-M {ECO:0000256|HAMAP-Rule:MF_01352};
GN Name=ndhM {ECO:0000256|HAMAP-Rule:MF_01352};
GN ORFNames=Cal7507_2122 {ECO:0000313|EMBL:AFY32564.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY32564.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY32564.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY32564.1,
RC ECO:0000313|Proteomes:UP000010390};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via
CC FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory
CC and/or the photosynthetic chain. The immediate electron acceptor for
CC the enzyme in this species is believed to be plastoquinone. Couples the
CC redox reaction to proton translocation, and thus conserves the redox
CC energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in
CC inorganic carbon-concentration. {ECO:0000256|HAMAP-Rule:MF_01352}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000256|ARBA:ARBA00001230, ECO:0000256|HAMAP-
CC Rule:MF_01352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000256|ARBA:ARBA00001558, ECO:0000256|HAMAP-
CC Rule:MF_01352};
CC -!- SUBUNIT: NDH-1 can be composed of about 15 different subunits;
CC different subcomplexes with different compositions have been identified
CC which probably have different functions. {ECO:0000256|HAMAP-
CC Rule:MF_01352}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01352}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01352}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01352}.
CC -!- SIMILARITY: Belongs to the complex I NdhM subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01352}.
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DR EMBL; CP003943; AFY32564.1; -; Genomic_DNA.
DR RefSeq; WP_015128378.1; NC_019682.1.
DR AlphaFoldDB; K9PIE8; -.
DR STRING; 99598.Cal7507_2122; -.
DR KEGG; calo:Cal7507_2122; -.
DR PATRIC; fig|99598.3.peg.2375; -.
DR eggNOG; ENOG5031AQM; Bacteria.
DR HOGENOM; CLU_137431_0_0_3; -.
DR OrthoDB; 461686at2; -.
DR Proteomes; UP000010390; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR HAMAP; MF_01352; NDH1_NDH1M; 1.
DR InterPro; IPR018922; NdhM.
DR PANTHER; PTHR36900; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT M, CHLOROPLASTIC; 1.
DR PANTHER; PTHR36900:SF1; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT M, CHLOROPLASTIC; 1.
DR Pfam; PF10664; NdhM; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01352};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01352};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01352};
KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957, ECO:0000256|HAMAP-
KW Rule:MF_01352};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_01352};
KW Reference proteome {ECO:0000313|Proteomes:UP000010390};
KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01352};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01352};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01352}.
SQ SEQUENCE 119 AA; 13546 MW; 662AE01B853802F0 CRC64;
MDNPTLLKST TRHIRIFAAE IDRGGELVPS NQVLTLDVDP DNEFNWNEDA LQKIYRKFDE
LVEASSGQDL TDYNLRRVGS DLEHYLRSLL QKGDISYNLS SRVTNYSMGL PQVAVAENQ
//
